Probing structure of neurotransmitter transporters by substituted-cysteine accessibility method

Methods Enzymol. 1998;296:331-46. doi: 10.1016/s0076-6879(98)96025-6.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Cysteine*
  • Dopamine / metabolism
  • Dopamine Plasma Membrane Transport Proteins
  • Humans
  • Kinetics
  • Membrane Glycoproteins*
  • Membrane Transport Proteins*
  • Models, Molecular
  • Mutagenesis, Site-Directed*
  • Nerve Tissue Proteins*
  • Neurotransmitter Agents / chemistry*
  • Neurotransmitter Agents / metabolism*
  • Protein Structure, Secondary*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sulfhydryl Reagents / pharmacology*
  • Transfection / methods

Substances

  • Carrier Proteins
  • Dopamine Plasma Membrane Transport Proteins
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • Recombinant Proteins
  • Sulfhydryl Reagents
  • Cysteine
  • Dopamine